ID Q9QJA3_9HIV1 Unreviewed; 347 AA.
AC Q9QJA3;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AAF08629.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAF08629.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAF08629.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAF08629.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10479129; DOI=10.1086/315017;
RA Brown A.J., Gunthard H.F., Wong J.K., D'Aquila R.T., Johnson V.A.,
RA Kuritzkes D.R., Richman D.D.;
RT "Sequence clusters in human immunodeficiency virus type 1 reverse
RT transcriptase are associated with subsequent virological response to
RT antiretroviral therapy.";
RL J. Infect. Dis. 180:1043-1049(1999).
RN [2] {ECO:0000313|EMBL:AAF08629.1}
RP NUCLEOTIDE SEQUENCE.
RA Leigh Brown A.J., Guenthard H.F., Wong J.K., D'Aquila R.T., Johnson V.A.,
RA Kuritzkes D.R., Richman D.D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAF08629.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10720511; DOI=10.1086/315329;
RA Hanna G.J., Johnson V.A., Kuritzkes D.R., Richman D.D., Brown A.J.,
RA Savara A.V., Hazelwood J.D., D'Aquila R.T.;
RT "Patterns of resistance mutations selected by treatment of human
RT immunodeficiency virus type 1 infection with zidovudine, didanosine, and
RT nevirapine.";
RL J. Infect. Dis. 181:904-911(2000).
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000256|RuleBase:RU004064}.
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DR EMBL; AF156046; AAF08629.1; -; Genomic_DNA.
DR PIR; A47330; A47330.
DR PIR; C47330; C47330.
DR PIR; D47330; D47330.
DR PIR; F47330; F47330.
DR PIR; S32132; S32132.
DR MEROPS; A02.001; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU004064};
KW DNA integration {ECO:0000256|ARBA:ARBA00023195};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|RuleBase:RU004064};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW Virion maturation {ECO:0000256|ARBA:ARBA00023113};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 26..95
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 149..339
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF08629.1"
FT NON_TER 347
FT /evidence="ECO:0000313|EMBL:AAF08629.1"
SQ SEQUENCE 347 AA; 39632 MW; 82882D17F1E1AD96 CRC64;
TVSFSFPQIT LWQRPLVTIK IGGQLKEALL DTGADDTVIE DMSLSGKWKP KMIGGIGGFI
KVRQYDQIPI EICGHKVIGT VLVGPTPVNI IGRNLWTQLG CTLNFPISPI ETVPVKLKPG
MDGPKVKQWP LTEEKIKALV EICTELEKEG KISKIGPENP YNTPIFAIKK KDGTKWRKLV
DFRELNKRTQ DFWEVQLGIP HPAGLKKKKS VTVLDVGDAY FSVPLDKDFR KYTAFTIPSI
NNETPGIRYQ YNVLPQGWKG SPAIFQSSMT KILEPFRKQN PDIVIYQYMD DLYVGSDLEI
EQHRTKIEEL RQHLGVWGFY TPDKKHQKEP PFLWMGYELH PDKWTVQ
//
